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At least 1,243 records · Page 69Linked to original sources
PubMed2002

Detection of knockdown resistance mutations in Anopheles sacharovi (Diptera: Culicidae) and genetic distance with Anopheles gambiae (Diptera: Culicidae) using cDNA sequencing of the voltage-gated sodium channel gene.

The knockdown resistance (kdr) mutation in the voltage-gated sodium channel gene (VGSCG), an important resistance mechanism against pyrethroids, was studied in Anopheles sacharovi Favre. It was found that the specific primers Agd1 and Agd2 used for polymerase chain reaction (PCR) amplification of Anopheles gambiae Giles VGSCG also amplified this genomic region in An. sacharovi. Comparison of the IIs4-IIs6 domain segments of the gene indicated 70% nucleotides common to both species and a genetic distance of 0.255 between them. Four different samples of pyrethroid-resistant An. sacharovi produced three types of amino acid, serine (TCG),leucine (TTG),and phenylalanine (TTT) at the kdr mutation point, whereas only two kdr mutations, leucine to phenylalanine and leucine to serine, occur in An. gambiae.

Animals↗
PubMed1999

Blue gourami (Trichogaster trichopterus) gonadotropic beta subunits (I and II) cDNA sequences and expression during oogenesis.

We have cloned two cDNAs from the pituitary gland of blue gourami (Trichogaster trichopterus), coding for the beta subunits of the gonadotropin hormones GtH-I and GtH-II. The two cDNAs were sequenced and subjected to sequence analysis. We have found that the deduced amino acid sequences of both cDNAs were most similar to their striped bass counterparts. The beta GtH-I subunits of blue gourami and striped bass shared 73% of their residues, and the beta GtH-II subunits 84%. The cloning of the cDNAs of beta GtH-I and beta GtH-II has enabled us to measure the expression of their respective mRNAs in the pituitaries of female blue gourami at different stages of the reproductive cycle. The highest levels of beta GtH-I and beta GtH-II mRNA were found in specimens classified as high vitellogenic and in females that were at the final stages of oocyte maturation.

Amino Acid Sequence↗
PubMed1991

Bovine and feline gastrin cDNA sequences and the amino acid and nucleotide sequence homologies among mammalian species.

The complete nucleotide sequences of cDNAs encoding bovine and feline preprogastrins have been cloned from the antral mucosa mRNA. The gastrin mRNA of each animal encodes a preprogastrin of 104 amino acids consisting of a signal peptide, a prosegment of 37 amino acids, and a gastrin 34 sequence, followed by a glycine (the amide donor). The cleavage following a pair of lysine residues yields gastrin 17. We found that pairs of arginine residues flanking gastrin 34, the typical processing site sequence of all other preprogastrins and many peptide hormones, were arginines in the bovine preprogastrin, but the first basic amino acid pair had changed to Arg-Trp (57-58 residues) instead of Arg-Arg in the feline preprogastrin. Comparison of these amino acid and nucleotide sequences with published mammalian sequences showed extensive homology in the coding (63 to 73% amino acid identity) and in the untranslated regions (67 to 89% identity). Prosequence, the most variable region, shows greater amino acid difference between bovine and human preprogastrin (54% identity), and between bovine and rat preprogastrin (54% identity) than between other species (62 to 82% identity).

Amino Acid Sequence↗
PubMed2000

Glycoprotein Ib-binding protein from the venom of Deinagkistrodon acutus--cDNA sequence, functional characterization, and three-dimensional modeling.

Agkicetin-C, a potent glycoprotein Ib antagonist from the venom of the Chinese pit viper, Deinagkistrodon acutus, has been purified and characterized (5). It is a disulfide-linked heterodimer containing subunits of 132 and of 123 amino acid residues. Herein, the complete amino acid sequences were resolved by cloning and nucleotide sequencing of the cDNAs. The sequences of its subunits are homologous to those of other snake venom proteins of the C-type (Ca2+-dependent) lectin superfamily. A three-dimensional model of agkicetin-C was constructed based on the crystal structure of habu coagulation factor IX/X-binding protein. By careful alignment of all the related sequences available and comparing the 3D-model of agkicetin-C with structures of other homologous proteins of different functions, some variable residues of agkicetin-C were identified, which possibly are responsible for the specificity of this distinct subtype of the C-type lectin-like venom proteins.

Amino Acid Sequence↗
PubMed2004

A monoclonal antibody against the paraneoplastic pemphigus (PNP) antigen, envoplakin: cDNA sequences encoding the variable regions of heavy and light chains.

Paraneoplastic pemphigus (PNP) is an acquired autoimmune disorder characterized by severe mucosal erosion, and polymorphous cutaneous lesions associated with neoplasia. PNP patients have circulating autoantibodies that bind to stratified and nonstratified epithelia. Previously, we showed that envoplakin was a component of the antigen complex recognized by PNP sera. In the present study we generated a monoclonal antibody, EVP-YS, against human envoplakin. The antibody bound to keratinocyte cell surfaces and reacted with the 210-kDa PNP antigen, confirming its specificity for envoplakin. The variable regions of the heavy (H) and light (L) chain genes were cloned from the hybridoma and shown to belong to mouse H chain subgroup III and kappa light chain subgroup V, respectively. The L chain of EVP-YS was 98% identical to the k chains of some autoantibodies and anti-nucleic acid antibodies, and had an identical amino acid sequence in all three complementary determining regions, suggesting that the H chains determine the specificity of the EVP-YS-envoplakin interaction. The EVP-YS antibody can be used to evaluate the sensitivity and specificity of clinical, histological, and immunological criteria for diagnosing PNP.

Animals↗
PubMed2006

[The study of ribosomal protein l15 cDNA sequences as a molecular marker in the teleostei phylogenetic analysis].

In this study, the full-length cDNAs of RPL15 (ribosomal protein L15) gene were cloned and sequenced from fifteen fishes of five orders under Teleostei. The complete ORF sequences were analyzed for phylogenetic reconstruction for the first time to evaluate the potential of RPL15 gene as a novel marker in resolving teleostean phylogenetic relationships. The resultant NJ, MP and ML trees with Anguilla japonica as the outgroup were generally resolved and largely congruent with the morphology-based tree though some incongruities were observed. The incongruities were then analyzed for some explanations. The results suggested that: (1) RPL15 gene was highly conserved during eukaryotic evolution; (2) RPL15 ORF might be a good phylogenetic marker for resolving teleostean relationships. It might be especially appropriate for the higher-level relationships (such as interordinal), and it was possibly suitable for lower-level relationships as well. The same can be true for other eukaryotes.

Animals↗
PubMed1992

Glucose transporter expression in brain. cDNA sequence of mouse GLUT3, the brain facilitative glucose transporter isoform, and identification of sites of expression by in situ hybridization.

Complementary DNAs encoding the mouse GLUT3/brain facilitative glucose transporter have been isolated and sequenced. The predicted amino acid sequence indicates that mouse GLUT3 is composed of 493 amino acids and has 83 and 89% identity and similarity, respectively, to the sequence of human GLUT3. In contrast to human GLUT3 mRNA, which can be readily detected by RNA blotting in all human tissues that have been examined, mouse GLUT3 mRNA was only present at significant levels in brain. In situ hybridization showed differential expression of GLUT3 mRNA in several regions of adult mouse brain. Specific expression was observed in the hippocampus, with GLUT3 mRNA levels being higher in areas CA1 to CA3 than in the dentate gyrus. It was also detected in the Purkinje cell layer of the cerebellum and in the cerebral cortex, with higher expression in the piriform cortex than in other regions of the cortex. Antisera to mouse GLUT3 immunoblotted a series of proteins of 45-50 kDa in mouse brain plasma membranes. These results are consistent with GLUT3 being a neuronal glucose transporter.

Amino Acid Sequence↗
PubMed1991

Casein kinase II. cDNA sequences, developmental expression, and tissue distribution of mRNAs for alpha, alpha', and beta subunits of the chicken enzyme.

We report the complete primary structures, as deduced from cloned cDNAs, of two catalytic (alpha and alpha') and one beta subunit of chicken casein kinase II. The alpha and alpha' subunits are closely related to each other but differ in their carboxyl termini; moreover, minor differences are distributed throughout the entire lengths of the two proteins, indicating that they are derived from separate genes. Comparison of the chicken protein sequences with those of their mammalian homologs reveals a high degree of evolutionary conservation of all three subunits. Northern analyses were carried out to study the expression of casein kinase II subunits during chicken embryonic development as well as in adult tissues. A single transcript migrating at 1 kilobase was detected when using a beta-specific probe, but multiple transcripts ranging in size from 1.45 to 2.8 kilobase were revealed by alpha- and alpha'-specific probes. Expression of mRNA for all three subunits was high in early embryos but decreased substantially during embryonic development. A comparative analysis of casein kinase II expression in different adult tissues revealed two major findings. First, relative levels of expression of the two catalytic subunits displayed a pronounced tissue specificity, consistent with the possibility that alpha and alpha' subunits may carry out specialized functions. Second, no correlation was observed between levels of transcripts for the catalytic subunits and those of mRNA for the beta subunit.

Amino Acid Sequence↗